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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Erythrocyte membrane protein band 4.1-like 2

4.1 g
Top mentioned proteins: 4.1B, 4.1N, Actin, CAN, V1a
Papers on 4.1 g
Protein 4.1G Regulates Cell Adhesion, Spreading and Migration of Mouse Embryo Fibroblasts through β1 Integrin Pathway.
New
An et al., Zhengzhou, China. In J Biol Chem, Jan 2016
UNASSIGNED: Protein 4.1G is a membrane skeletal protein that can serve as adapter between transmembrane proteins and the underlying membrane skeleton.
Involvement of membrane skeletal molecules in the Schmidt-Lanterman incisure in Schwann cells.
New
Ohno et al., Matsumoto, Japan. In Med Mol Morphol, Dec 2015
An analogous molecular complex, 4.1G-MPP6-cell adhesion molecule 4 (CADM4), is incorporated into the Schmidt-Lanterman incisure (SLI), a truncated cone shape in the myelin internode that is a specific feature of myelinated nerve fibers formed in Schwann cells in the peripheral nervous system.
Immunohistochemical study of the membrane skeletal protein, membrane protein palmitoylated 6 (MPP6), in the mouse small intestine.
New
Terada et al., Matsumoto, Japan. In Histochem Cell Biol, Nov 2015
We previously described the interaction of another MPP family, MPP6, with 4.1G in the mouse peripheral nervous system.
Protein-4.1G-Mediated Membrane Trafficking Is Essential for Correct Rod Synaptic Location in the Retina and for Normal Visual Function.
New
Furukawa et al., Suita, Japan. In Cell Rep, Mar 2015
We show here that a membrane scaffold protein, 4.1G, is highly expressed in retinal photoreceptors and is essential for the arrangement of their correct synapse location.
Comprehensive characterization of protein 4.1 expression in epithelium of large intestine.
An et al., Beijing, China. In Histochem Cell Biol, 2014
The protein 4.1 family consists of four members, 4.1R, 4.1N, 4.1B and 4.1G, each encoded by a distinct gene.
Immunohistochemical study of mouse sciatic nerves under various stretching conditions with "in vivo cryotechnique".
Terada et al., Matsumoto, Japan. In J Neurosci Methods, 2014
Immunolocalizations of protein 4.1G and albumin were also examined in the fibers.
The Protein 4.1 family: hub proteins in animals for organizing membrane proteins.
Review
Bennett et al., London, United Kingdom. In Biochim Biophys Acta, 2014
Vertebrates have four paralogues, known as 4.1R, 4.1N, 4.1G and 4.1B, which are additionally duplicated in the ray-finned fish.
Interaction of 4.1G and cGMP-gated channels in rod photoreceptor outer segments.
Molday et al., Vancouver, Canada. In J Cell Sci, 2014
Using immunoprecipitation and mass spectrometry, 4.1G was identified as a new interacting partner for the cyclic-nucleotide gated (CNG) channels in ROSs.
Cortical dynein and asymmetric membrane elongation coordinately position the spindle in anaphase.
Impact
Cheeseman et al., Cambridge, United States. In Cell, 2013
First, the spindle is positioned directly by the microtubule-based motor dynein, which we demonstrate is targeted to the cell cortex by two distinct pathways: a Gαi/LGN/NuMA-dependent pathway and a 4.1G/R and NuMA-dependent, anaphase-specific pathway.
Novel mechanism of regulation of protein 4.1G binding properties through Ca2+/calmodulin-mediated structural changes.
Takakuwa et al., Akita, Japan. In Cell Biochem Biophys, 2013
Protein 4.1G (4.1G) is a widely expressed member of the protein 4.1 family of membrane skeletal proteins.
Functional characterization of protein 4.1 homolog in amphioxus: defining a cryptic spectrin-actin-binding site.
Zhang et al., Qingdao, China. In Sci Rep, 2012
We also showed that amphioxus 4.1 protein gene was the common ancestor of vertebrate 4.1 protein genes, from which 4.1R, 4.1N, 4.1G, and 4.1B genes originated.
Isoforms of protein 4.1 are differentially distributed in heart muscle cells: relation of 4.1R and 4.1G to components of the Ca2+ homeostasis system.
GeneRIF
Baines et al., London, United Kingdom. In Exp Cell Res, 2012
4.1G existed in an immunoprecipitable complex with spectrin and SERCA2.
The cytoskeletal adapter protein 4.1G organizes the internodes in peripheral myelinated nerves.
GeneRIF
Peles et al., Göttingen, Germany. In J Cell Biol, 2012
protein 4.1G contributes to the organization of the internodal axolemma by targeting and/or maintaining glial transmembrane proteins along the axoglial interface
Serine phosphorylation of FcγRI cytoplasmic domain directs lipid raft localization and interaction with protein 4.1G.
GeneRIF
Kimberly et al., Birmingham, United States. In J Leukoc Biol, 2012
A phosphoserine-dependent tethering role for protein 4.1G in lipid rafts provides insight into the unique phosphoserine-based regulation of FcgammaRI receptor signaling.
Essential function of protein 4.1G in targeting of membrane protein palmitoylated 6 into Schmidt-Lanterman incisures in myelinated nerves.
GeneRIF
Ohno et al., Japan. In Mol Cell Biol, 2012
In the mouse sciatic nerve, protein 4.1G colocalized at Schmidt-Lanterman incisures (SLI) and the paranodes with a member of the membrane-associated guanylate kinase (MAGUK) family, membrane protein palmitoylated 6.
Lack of protein 4.1G causes altered expression and localization of the cell adhesion molecule nectin-like 4 in testis and can cause male infertility.
GeneRIF
An et al., New York City, United States. In Mol Cell Biol, 2011
findings imply that 4.1G plays a role in spermatogenesis by mediating cell-cell adhesion between spermatogenic and Sertoli cells through its interaction with NECL4 on Sertoli cells
Protein 4.1 and the control of ion channels.
Review
Terracciano et al., Canterbury, United Kingdom. In Blood Cells Mol Dis, 2009
4.1R is one member of the mammalian 4.1 family - the others being 4.1N, 4.1G and 4.1B - and is expressed in many cell types other than erythrocytes.
[Regulation of G protein-coupled receptor function by its binding proteins].
Review
Saito et al., Sendai, Japan. In Yakugaku Zasshi, 2007
We identified t-complex testis expressed-1 (Tctex-1) and 4.1G as associated proteins for the PTHR.
Protein 4.1, a component of the erythrocyte membrane skeleton and its related homologue proteins forming the protein 4.1/FERM superfamily.
Review
Sikorski et al., Wrocław, Poland. In Folia Histochem Cytobiol, 2005
Non-erythroid cells express the 4.1R homologues: 4.1G (general type), 4.1B (brain type), and 4.1N (neuron type), and the whole group belongs to the protein 4.1 superfamily, which is characterized by the presence of a highly conserved FERM domain at the N-terminus of the molecule.
Protein 4.1, a multifunctional protein of the erythrocyte membrane skeleton: structure and functions in erythrocytes and nonerythroid cells.
Review
Takakuwa, Tokyo, Japan. In Int J Hematol, 2000
This review introduces current knowledge on biochemical, biophysical, genetic, and functional aspects of 4.1R and its family proteins, 4.1G (general type), 4.1B (brain type), and 4.1N (neuron type), recently identified in nonerythroid cells.
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